Specific monovalent cation effect on protein-protein interactions revealed by protein rotational diffusion analysis

Akane Kato, Yudai Katsuki, Etsuko Nishimoto

Research output: Contribution to journalArticle

Abstract

The protein-protein interactions induced by cation specific effects were characterized by the rotational diffusion analysis. The rotational diffusion coefficient, Drot, estimated by time-resolved fluorescence anisotropy of fluorescent-labeled lysozyme was reduced responding to monovalent cation chlorides and was able to be approximated by quadratic functions of lysozyme concentration. The resultant first and second terms of lysozyme concentration were observed to be negative and positive according to the species and concentrations of monovalent cations, respectively. These two hydrodynamic interaction parameters demonstrated that the attractive and also repulsive interactions were induced between lysozymes in the order of inverse Hofmeister effect.

Original languageEnglish
Pages (from-to)89-94
Number of pages6
JournalChemical Physics Letters
Volume730
DOIs
Publication statusPublished - Sep 1 2019

Fingerprint

Monovalent Cations
lysozyme
Muramidase
proteins
cations
Proteins
interactions
Cations
Chlorides
Anisotropy
Hydrodynamics
diffusion coefficient
Fluorescence
chlorides
hydrodynamics
fluorescence
anisotropy

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

Cite this

Specific monovalent cation effect on protein-protein interactions revealed by protein rotational diffusion analysis. / Kato, Akane; Katsuki, Yudai; Nishimoto, Etsuko.

In: Chemical Physics Letters, Vol. 730, 01.09.2019, p. 89-94.

Research output: Contribution to journalArticle

@article{075c45a76bf44cda824a998f44eea73c,
title = "Specific monovalent cation effect on protein-protein interactions revealed by protein rotational diffusion analysis",
abstract = "The protein-protein interactions induced by cation specific effects were characterized by the rotational diffusion analysis. The rotational diffusion coefficient, Drot, estimated by time-resolved fluorescence anisotropy of fluorescent-labeled lysozyme was reduced responding to monovalent cation chlorides and was able to be approximated by quadratic functions of lysozyme concentration. The resultant first and second terms of lysozyme concentration were observed to be negative and positive according to the species and concentrations of monovalent cations, respectively. These two hydrodynamic interaction parameters demonstrated that the attractive and also repulsive interactions were induced between lysozymes in the order of inverse Hofmeister effect.",
author = "Akane Kato and Yudai Katsuki and Etsuko Nishimoto",
year = "2019",
month = "9",
day = "1",
doi = "10.1016/j.cplett.2019.05.019",
language = "English",
volume = "730",
pages = "89--94",
journal = "Chemical Physics Letters",
issn = "0009-2614",
publisher = "Elsevier",

}

TY - JOUR

T1 - Specific monovalent cation effect on protein-protein interactions revealed by protein rotational diffusion analysis

AU - Kato, Akane

AU - Katsuki, Yudai

AU - Nishimoto, Etsuko

PY - 2019/9/1

Y1 - 2019/9/1

N2 - The protein-protein interactions induced by cation specific effects were characterized by the rotational diffusion analysis. The rotational diffusion coefficient, Drot, estimated by time-resolved fluorescence anisotropy of fluorescent-labeled lysozyme was reduced responding to monovalent cation chlorides and was able to be approximated by quadratic functions of lysozyme concentration. The resultant first and second terms of lysozyme concentration were observed to be negative and positive according to the species and concentrations of monovalent cations, respectively. These two hydrodynamic interaction parameters demonstrated that the attractive and also repulsive interactions were induced between lysozymes in the order of inverse Hofmeister effect.

AB - The protein-protein interactions induced by cation specific effects were characterized by the rotational diffusion analysis. The rotational diffusion coefficient, Drot, estimated by time-resolved fluorescence anisotropy of fluorescent-labeled lysozyme was reduced responding to monovalent cation chlorides and was able to be approximated by quadratic functions of lysozyme concentration. The resultant first and second terms of lysozyme concentration were observed to be negative and positive according to the species and concentrations of monovalent cations, respectively. These two hydrodynamic interaction parameters demonstrated that the attractive and also repulsive interactions were induced between lysozymes in the order of inverse Hofmeister effect.

UR - http://www.scopus.com/inward/record.url?scp=85066272550&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85066272550&partnerID=8YFLogxK

U2 - 10.1016/j.cplett.2019.05.019

DO - 10.1016/j.cplett.2019.05.019

M3 - Article

AN - SCOPUS:85066272550

VL - 730

SP - 89

EP - 94

JO - Chemical Physics Letters

JF - Chemical Physics Letters

SN - 0009-2614

ER -